Acetohydroxy acid synthase I, a required enzyme for isoleucine and valine biosynthesis in Escherichia coli K-12 during growth on acetate as the sole carbon source
about
PdhR, the pyruvate dehydrogenase repressor, does not regulate lipoic acid synthesis.Multiple copies of a bile acid-inducible gene in Eubacterium sp. strain VPI 12708Acetohydroxy acid synthase activity from a mutation at ilvF in Escherichia coli K-12Acetohydroxy acid synthase I is required for isoleucine and valine biosynthesis by Salmonella typhimurium LT2 during growth on acetate or long-chain fatty acids.Alkylation of acetohydroxyacid synthase I from Escherichia coli K-12 by 3-bromopyruvate: evidence for a single active site catalyzing acetolactate and acetohydroxybutyrate synthesisProtein Profiling Reveals Novel Proteins in Pollen and Pistil of W22 (ga1; Ga1) in Maize.Characterization of TPP-binding proteins in Methanococci archaeal species.A kinetic platform for in silico modeling of the metabolic dynamics in Escherichia coli.Characterization of acetohydroxyacid synthase I from Escherichia coli K-12 and identification of its inhibitors.Global transcriptomic analysis of an engineered Escherichia coli strain lacking the phosphoenolpyruvate: carbohydrate phosphotransferase system during shikimic acid production in rich culture mediumProtein trans-splicing to produce herbicide-resistant acetolactate synthase.Branched-chain amino acid biosynthesis in Salmonella typhimurium: a quantitative analysisProperties of subcloned subunits of bacterial acetohydroxy acid synthases.Physiological implications of the substrate specificities of acetohydroxy acid synthases from varied organisms.Physiological implications of the specificity of acetohydroxy acid synthase isozymes of enteric bacteria.Conversion of Escherichia coli pyruvate oxidase to an 'alpha-ketobutyrate oxidase'.Zinc inhibition of protein trans-splicing and identification of regions essential for splicing and association of a split intein*.Many of the functional differences between acetohydroxyacid synthase (AHAS) isozyme I and other AHASs are a result of the rapid formation and breakdown of the covalent acetolactate-thiamin diphosphate adduct in AHAS I.Molecular evolution of acetohydroxyacid synthase in bacteria.Quantifying the entropic cost of cellular growth control.Making metabolism accessible and meaningful: is the definition of a central metabolic dogma within reach?
P2860
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P2860
Acetohydroxy acid synthase I, a required enzyme for isoleucine and valine biosynthesis in Escherichia coli K-12 during growth on acetate as the sole carbon source
description
1986 nî lūn-bûn
@nan
1986 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1986 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1986年の論文
@ja
1986年論文
@yue
1986年論文
@zh-hant
1986年論文
@zh-hk
1986年論文
@zh-mo
1986年論文
@zh-tw
1986年论文
@wuu
name
Acetohydroxy acid synthase I, ...... tate as the sole carbon source
@ast
Acetohydroxy acid synthase I, ...... tate as the sole carbon source
@en
Acetohydroxy acid synthase I, ...... tate as the sole carbon source
@nl
type
label
Acetohydroxy acid synthase I, ...... tate as the sole carbon source
@ast
Acetohydroxy acid synthase I, ...... tate as the sole carbon source
@en
Acetohydroxy acid synthase I, ...... tate as the sole carbon source
@nl
prefLabel
Acetohydroxy acid synthase I, ...... tate as the sole carbon source
@ast
Acetohydroxy acid synthase I, ...... tate as the sole carbon source
@en
Acetohydroxy acid synthase I, ...... tate as the sole carbon source
@nl
P2860
P1476
Acetohydroxy acid synthase I, ...... tate as the sole carbon source
@en
P2093
F E Dailey
J E Cronan
P2860
P304
P356
10.1128/JB.165.2.453-460.1986
P407
P577
1986-02-01T00:00:00Z